The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum

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dc.contributor.author Esteban-Torres, María
dc.contributor.author Reverón, Inés
dc.contributor.author Santamaría, Laura
dc.contributor.author Mancheño, José M.
dc.contributor.author de las Rivas, Blanca
dc.contributor.author Muñoz, Rosario
dc.date.accessioned 2017-06-20T11:39:45Z
dc.date.available 2017-06-20T11:39:45Z
dc.date.issued 2016-07-19
dc.identifier.citation Esteban-Torres, M., Reverón, I., Santamaría, L., Mancheño, J. M., de las Rivas, B. and Muñoz, R. (2016) 'The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum', Frontiers in Microbiology, 7,1118 (10pp). doi: 10.3389/fmicb.2016.01118 en
dc.identifier.volume 7
dc.identifier.startpage 1
dc.identifier.endpage 10
dc.identifier.issn 1664-302X
dc.identifier.uri http://hdl.handle.net/10468/4111
dc.identifier.doi 10.3389/fmicb.2016.01118
dc.description.abstract Lactobacillus plantarum species is a good source of esterases since both lipolytic and esterase activities have been described for strains of this species. No fundamental biochemical difference exists among esterases and lipases since both share a common catalytic mechanism. L. plantarum WCFS1 possesses a protein, Lp_3561, which is 44% identical to a previously described lipase, Lp_3562. In contrast to Lp_3562, Lp_3561 was unable to degrade esters possessing a chain length higher than C4 and the triglyceride tributyrin. As in other L. plantarum esterases, the electrostatic potential surface around the active site in Lp_3561 is predicted to be basic, whereas it is essentially neutral in the Lp_3562 lipase. The fact that the genes encoding both proteins were located contiguously in the L. plantarum WCFS1 genome, suggests that they originated by tandem duplication, and therefore are paralogs as new functions have arisen during evolution. The presence of the contiguous lp_3561 and lp_3562 genes was studied among L. plantarum strains. They are located in a 8,903 bp DNA fragment that encodes proteins involved in the catabolism of sialic acid and are predicted to increase bacterial adaptability under certain growth conditions. en
dc.description.sponsorship Ministerio de Economía y Competitividad(AGL2014-52911R; AGL2011-22745); Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (RM2012-00004). en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher Frontiers Media en
dc.relation.uri http://journal.frontiersin.org/article/10.3389/fmicb.2016.01118/full
dc.rights © 2016, Esteban-Torres, Reverón, Santamaría, Mancheño, de las Rivas and Muñoz. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.subject Esterase en
dc.subject Lipase en
dc.subject Electrostatic potential surface en
dc.subject Tandem duplication en
dc.subject Paralog genes en
dc.subject Lactic acid bacteria en
dc.subject Genomic island en
dc.title The Lp_3561 and Lp_3562 enzymes support a functional divergence process in the lipase/esterase toolkit from Lactobacillus plantarum en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother María Esteban-Torres, APC Microbiome Institute, Microbiology, University College Cork, Cork, Ireland. +353-21-490-3000 Email: maria.estebantorres@umail.ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Ministerio de Economía y Competitividad
dc.contributor.funder Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria
dc.description.status Peer reviewed en
dc.identifier.journaltitle Frontiers in Microbiology en
dc.internal.IRISemailaddress maria.estebantorres@umail.ucc.ie en
dc.identifier.articleid 1118


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© 2016, Esteban-Torres, Reverón, Santamaría, Mancheño, de las Rivas and Muñoz. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms Except where otherwise noted, this item's license is described as © 2016, Esteban-Torres, Reverón, Santamaría, Mancheño, de las Rivas and Muñoz. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms
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